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| | <StructureSection load='2xus' size='340' side='right'caption='[[2xus]], [[Resolution|resolution]] 1.91Å' scene=''> | | <StructureSection load='2xus' size='340' side='right'caption='[[2xus]], [[Resolution|resolution]] 1.91Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xus]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XUS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xus]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XUS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.912Å</td></tr> |
| | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xus OCA], [https://pdbe.org/2xus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xus RCSB], [https://www.ebi.ac.uk/pdbsum/2xus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xus ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xus OCA], [https://pdbe.org/2xus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xus RCSB], [https://www.ebi.ac.uk/pdbsum/2xus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xus ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/BRMS1_HUMAN BRMS1_HUMAN]] Transcriptional repressor. Down-regulates transcription activation by NF-kappa-B by promoting the deacetylation of RELA at 'Lys-310'. Promotes HDAC1 binding to promoter regions. Down-regulates expression of anti-apoptotic genes that are controlled by NF-kappa-B. Promotes apoptosis in cells that have inadequate adherence to a substrate, a process called anoikis, and may thereby inhibit metastasis. May be a mediator of metastasis suppression in breast carcinoma.<ref>PMID:14581478</ref> <ref>PMID:17000776</ref> <ref>PMID:20830743</ref>
| + | [https://www.uniprot.org/uniprot/BRMS1_HUMAN BRMS1_HUMAN] Transcriptional repressor. Down-regulates transcription activation by NF-kappa-B by promoting the deacetylation of RELA at 'Lys-310'. Promotes HDAC1 binding to promoter regions. Down-regulates expression of anti-apoptotic genes that are controlled by NF-kappa-B. Promotes apoptosis in cells that have inadequate adherence to a substrate, a process called anoikis, and may thereby inhibit metastasis. May be a mediator of metastasis suppression in breast carcinoma.<ref>PMID:14581478</ref> <ref>PMID:17000776</ref> <ref>PMID:20830743</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bravo, J]] | + | [[Category: Bravo J]] |
| - | [[Category: Neira, J L]] | + | [[Category: Neira JL]] |
| - | [[Category: Ortiz-Lombardia, M]] | + | [[Category: Ortiz-Lombardia M]] |
| - | [[Category: Rivera, J]] | + | [[Category: Rivera J]] |
| - | [[Category: Romero, A]] | + | [[Category: Romero A]] |
| - | [[Category: Spinola-Amilibia, M]] | + | [[Category: Spinola-Amilibia M]] |
| - | [[Category: Breast cancer metastasis]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
BRMS1_HUMAN Transcriptional repressor. Down-regulates transcription activation by NF-kappa-B by promoting the deacetylation of RELA at 'Lys-310'. Promotes HDAC1 binding to promoter regions. Down-regulates expression of anti-apoptotic genes that are controlled by NF-kappa-B. Promotes apoptosis in cells that have inadequate adherence to a substrate, a process called anoikis, and may thereby inhibit metastasis. May be a mediator of metastasis suppression in breast carcinoma.[1] [2] [3]
Publication Abstract from PubMed
We present here the first structural report derived from breast cancer metastasis suppressor 1 (BRMS1), a member of the metastasis suppressor protein group, which, during recent years, have drawn much attention since they suppress metastasis without affecting the growth of the primary tumor. The relevance of the predicted N-terminal coiled coil on the molecular recognition of some of the BRMS1 partners, on its cellular localization and on the role of BRMS1 biological functions such as transcriptional repression prompted us to characterize its three-dimensional structure by X-ray crystallography. The structure of BRMS1 N-terminal region reveals that residues 51-98 form an antiparallel coiled-coil motif and, also, that it has the capability of homo-oligomerizing in a hexameric conformation by forming a trimer of coiled-coil dimers. We have also performed hydrodynamic experiments that strongly supported the prevalence in solution of this quaternary structure for BRMS1(51-98). This work explores the structural features of BRMS1 N-terminal region to help clarify the role of this area in the context of the full-length protein. Our crystallographic and biophysical results suggest that the biological function of BRMS1 may be affected by its ability to promote molecular clustering through its N-terminal coiled-coil region.
The Structure of BRMS1 Nuclear Export Signal and SNX6 Interacting Region Reveals a Hexamer Formed by Antiparallel Coiled Coils.,Spinola-Amilibia M, Rivera J, Ortiz-Lombardia M, Romero A, Neira JL, Bravo J J Mol Biol. 2011 Sep 2;411(5):1114-27. Epub 2011 Jul 18. PMID:21777593[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Meehan WJ, Samant RS, Hopper JE, Carrozza MJ, Shevde LA, Workman JL, Eckert KA, Verderame MF, Welch DR. Breast cancer metastasis suppressor 1 (BRMS1) forms complexes with retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone deacetylase complex and represses transcription. J Biol Chem. 2004 Jan 9;279(2):1562-9. Epub 2003 Oct 26. PMID:14581478 doi:http://dx.doi.org/10.1074/jbc.M307969200
- ↑ Liu Y, Smith PW, Jones DR. Breast cancer metastasis suppressor 1 functions as a corepressor by enhancing histone deacetylase 1-mediated deacetylation of RelA/p65 and promoting apoptosis. Mol Cell Biol. 2006 Dec;26(23):8683-96. Epub 2006 Sep 25. PMID:17000776 doi:10.1128/MCB.00940-06
- ↑ Rivera J, Megias D, Bravo J. Sorting nexin 6 interacts with breast cancer metastasis suppressor-1 and promotes transcriptional repression. J Cell Biochem. 2010 Dec 15;111(6):1464-72. doi: 10.1002/jcb.22874. PMID:20830743 doi:http://dx.doi.org/10.1002/jcb.22874
- ↑ Spinola-Amilibia M, Rivera J, Ortiz-Lombardia M, Romero A, Neira JL, Bravo J. The Structure of BRMS1 Nuclear Export Signal and SNX6 Interacting Region Reveals a Hexamer Formed by Antiparallel Coiled Coils. J Mol Biol. 2011 Sep 2;411(5):1114-27. Epub 2011 Jul 18. PMID:21777593 doi:10.1016/j.jmb.2011.07.006
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